BMRB Entry 50410

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50410

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR signal assignments and backbone dynamics of the apo-C-terminal domain of orange carotenoid protein from cyanobacteria
Deposition date:
2020-07-25
Original release date:
2020-11-03
Authors:
Maksimov, Eugene; Slonimskiy, Yury; Laptev, Gennady; Blokhin, Dmitry; Chang, Chi-Fon; Friedrich, Thomas; Sluchanko, Nikolai; Polshakov, Vladimir
Citation:

Citation: Maksimov, Eugene; Laptev, Gennady Yu; Blokhin, Dmitriy; Klochkov, Vladimir; Slonimskiy, Yury; Sluchanko, Nikolai; Friedrich, Thomas; Chang, Chi-Fon; Polshakov, Vladimir. "NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein"  Biomol. NMR Assign. 15, 17-23 (2021).
PubMed: 32939684

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Anabaena sp.   Taxonomy ID: 1167   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Anabaena Anabaena sp.

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCDFDuet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGKAAESLPNIQIKSIAGIT EPTILQYFATLNAGEFAATA ALFAVDGVMYPPFESGIVGP DAIAAYLQQEAQGIKAEPQQ GLAETSEDGHTQVQVSGKAQ TSWCGVNVLWLFTLNQEKQI IHTQIKLLASPQELLALRRE QHHHHHHH

Data sets:
Data typeCount
13C chemical shifts496
15N chemical shifts129
1H chemical shifts881
T1 relaxation values108
T2 relaxation values108
heteronuclear NOE values108

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ApoCTDH1

Entities:

Entity 1, ApoCTDH 148 residues - Formula weight is not available

1   METGLYLYSALAALAGLUSERLEUPROASN
2   ILEGLNILELYSSERILEALAGLYILETHR
3   GLUPROTHRILELEUGLNTYRPHEALATHR
4   LEUASNALAGLYGLUPHEALAALATHRALA
5   ALALEUPHEALAVALASPGLYVALMETTYR
6   PROPROPHEGLUSERGLYILEVALGLYPRO
7   ASPALAILEALAALATYRLEUGLNGLNGLU
8   ALAGLNGLYILELYSALAGLUPROGLNGLN
9   GLYLEUALAGLUTHRSERGLUASPGLYHIS
10   THRGLNVALGLNVALSERGLYLYSALAGLN
11   THRSERTRPCYSGLYVALASNVALLEUTRP
12   LEUPHETHRLEUASNGLNGLULYSGLNILE
13   ILEHISTHRGLNILELYSLEULEUALASER
14   PROGLNGLULEULEUALALEUARGARGGLU
15   GLNHISHISHISHISHISHISHIS

Samples:

sample_1: ApoCTDH, [U-99% 13C; U-99% 15N], 0.5 ± 0.1 mM; sodium phosphate 40 ± 0.1 mM; sodium azide 0.02%; dithiothreitol 2.7 ± 0.01 mM

sample_2: ApoCTDH, [U-99% 13C; U-99% 15N], 0.5 ± 0.1 mM; sodium phosphate 40 ± 0.1 mM; sodium azide 0.02%; dithiothreitol 2.7 ± 0.01 mM

sample_3: ApoCTDH, [U-99% 15N], 0.6 ± 0.1 mM; sodium phosphate 40 ± 0.1 mM; sodium azide 0.02%; dithiothreitol 2.7 ± 0.01 mM

sample_4: ApoCTDH 0.8 ± 0.1 mM; sodium phosphate 40 ± 0.1 mM; sodium azide 0.02%; dithiothreitol 2.7 ± 0.01 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
1H-15N heteronoesample_3isotropicsample_conditions_1
T1/R1 relaxationsample_3isotropicsample_conditions_1
T2/R2 relaxationsample_3isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - data analysis

PINE - chemical shift assignment

TALOS+ - data analysis

RelaxFit - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Bruker AVANCE III 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks